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ProteomicsSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 2)
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0–SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structural–pr...
ORGANISM(S): Homo sapiens (Human) 
2017-01-24 | PXD005296 | Pride
Sumo Phosphorylation Deep Proteome K0-sumo 
ProteomicsSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 1)
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0–SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structural–pr...
ORGANISM(S): Homo sapiens (Human) 
2017-01-24 | PXD004927 | Pride
Sumo Phosphorylation Deep Proteome K0-sumo 
UnknownArabidopsis-expressing lysine-null SUMO1 reveals a non-essential role for secondary SUMO modifications in plants.
Not available
S-EPMC10350450 | biostudies-literature
ProteomicsA ZNF-nanobody fusion reveals SUMOylation-dependent changes in protein localization
SUMOylation is a post-translational modification regulating protein localization, stability, and activity, with effects varying depending on the identity of the conjugated SUMO protein (SUMO1 or SUMO2/3) and type of SUMOylation (mono-, multi-, or poly-). We previously developed a small 32 amino acid...
ORGANISM(S): Homo sapiens (Human) 
2026-03-24 | PXD069854 | Pride
ProteomicsUncovering Global SUMOylation Signaling Networks in a Site-Specific Manner
SUMOylation is a reversible post-translational modification essential for genome stability. Using high-resolution mass spectrometry, we have studied global SUMOylation in mammalian cells and in a site-specific manner, identifying a total of over 4,300 SUMOylation sites in over 1,600 proteins. Moreov...
ORGANISM(S): Homo sapiens (Human) 
2014-09-04 | PXD001061 | Pride
Sumo-2 Qqtgg Sumo Sumo2 Q87r 
ProteomicsSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 2)
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0â??SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structuralâ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-04-01 | MSV000080869 | MassIVE
ProteomicsSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 1)
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0â??SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structuralâ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-30 | MSV000080812 | MassIVE
ProteomicsSUMO-2 Orchestrates Chromatin Modifiers in Response to DNA Damage
Small Ubiquitin-like Modifiers play critical roles in the DNA Damage Response (DDR). To increase our understanding of SUMOylation in the mammalian DDR, we employed a quantitative proteomics approach to identify dynamically regulated SUMO-2 conjugates and modification sites upon treatment with the DN...
ORGANISM(S): Homo sapiens (Human) 
2015-03-16 | PXD001810 | Pride
Dna Damage Mms Sumo-2 Sumo Chromatin Repair Site 
ProteomicsChromokinesin KIF4A teams up with STMN1 to regulate abscission in a SUMO-dependent manner
Cell division ends when two daughter cells physically separate via abscission, the cleavage of the intercellular bridge. It is currently less clear how the anti-parallel microtubule bundles bridging daughter cells are severed. Here, we provide evidence for a novel abscission mechanism. We found that...
ORGANISM(S): Homo sapiens (Human) 
2020-07-14 | PXD007055 | Pride
Cytokinesis Abscission Kif4a Mitosis Human Stmn1 Sumo Lc-ms/ms 
ProteomicsSUMO-2 activity is inhibited by non-covalent interactions with the Aβ peptide: an exploration of potential pathogenic mechanisms in Alzheimer’s Disease
SUMOylation is a post-translational modification involving the addition of SUMO isoforms to target proteins and plays a role in various biological processes, including neurodegenerative diseases and ocular pathologies. This study investigates the interaction between SUMO-2 and amyloid (Aβ) peptides,...
ORGANISM(S): Homo sapiens (Human) 
2025-08-25 | PXD066055 | Pride
Aβ Protein protein interactions Crosslinking ms Alzheimer’s disease Xl-ms Sumo-2 Cross-linking mass spectrometry 
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